STC1

Last updated
STC1
Identifiers
Aliases STC1 , STC, stanniocalcin 1
External IDs OMIM: 601185 MGI: 109131 HomoloGene: 2374 GeneCards: STC1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003155

NM_009285

RefSeq (protein)

NP_003146

NP_033311

Location (UCSC) Chr 8: 23.84 – 23.85 Mb Chr 14: 69.27 – 69.28 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Stanniocalcin-1 is a glycoprotein, a homologue of a hormone stanniocalcin, first discovered in bony fishes. In humans it is encoded by the STC1 gene. [5] [6]

Contents

Function

This gene encodes a secreted, homodimeric glycoprotein that is expressed in a wide variety of tissues and may have autocrine or paracrine functions. The only known molecular function of human Stanniocalcin-1 to date is a SUMO E3 ubiquitin ligase activity in the SUMOylation cycle. However, STC1 interacts with many proteins in the cytoplasm, mitochondria, endoplasmatic reticulum, and in dot-like fashion in the cell nucleus. The N-terminal region of STC1 is the function region which is responsible to establish the interaction with its partners, including SUMO1. [7] Low-resolution studies shows that STC1 is an anti-parallel homodimer in solution and the cysteine 202 is responsible for its dimerization. All the 5 disulfide bonds of human STC1 are conserved and have the same profile of fish STC. [8] The gene contains a 5' UTR rich in CAG trinucleotide repeats. The encoded protein contains 11 conserved cysteine residues and is phosphorylated by protein kinase C exclusively on its serine residues.

The protein may play a role in the regulation of renal and intestinal calcium and phosphate transport, cell metabolism, or cellular calcium/phosphate homeostasis. Overexpression of human stanniocalcin 1 in mice produces high serum phosphate levels, dwarfism, and increased metabolic rate. This gene has altered expression in hepatocellular, ovarian, and breast cancers, [6] and is a putative molecular biomarker of leukemic microenvironment.

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Stanniocalcin is a family of hormones which regulate calcium and phosphate balance in the body. The first stanniocalcin discovered was from fish and was identified as the principal calcium-reducing (hypocalcaemic) factor. It was isolated from special organs in fish called corpuscles of Stannius, hence the name stanniocalcin. Chemically, stanniocalcins are glycosylated proteins having a molecular mass of 50 kDa. They exist in molecular pairs (homodimers) and are joined together by disulfide linkage. Stanniocalcins are made up of approximately 250 amino acids.

Corpuscle of Stannius Special endocrine organs in the kidney in fish

The corpuscles of Stannius are special endocrine organs in the kidney in fish and are responsible for maintaining calcium balance. They are found only in bony fishes. They were discovered and described by a German anatomist Hermann Friedrich Stannius in 1839. Stannius considered them as functionally similar to adrenal glands in mammals. But they have later been found to be anatomically different as they are derived from different tissues of the embryo. Structurally the corpuscles are a large number of spherical bodies separated from each other by loose connective tissues. Each body or lobule is in turn composed of several columnar cells, which contain secretory granules and are, thus, secretory in function. Each Secretory granule is spherical in shape and measures 0.5 to 1 μm in diameter. Their possible endocrine nature, i.e. producing hormone, was suspected from the complete anatomical description, and it was believed to be responsible for regulating calcium level in the blood. The hormone was identified as stanniocalcin.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000159167 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000014813 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Chang AC, Jeffrey KJ, Tokutake Y, Shimamoto A, Neumann AA, Dunham MA, Cha J, Sugawara M, Furuichi Y, Reddel RR (Feb 1998). "Human stanniocalcin (STC): genomic structure, chromosomal localization, and the presence of CAG trinucleotide repeats". Genomics. 47 (3): 393–8. doi:10.1006/geno.1997.5120. PMID   9480753.
  6. 1 2 "Entrez Gene: STC1 stanniocalcin 1".
  7. dos Santos MT, Trindade DM, Gonçalves Kde A, Bressan GC, Anastassopoulos F, Yunes JA, Kobarg J (Jan 2011). "Human stanniocalcin-1 interacts with nuclear and cytoplasmic proteins and acts as a SUMO E3 ligase". Molecular BioSystems. 7 (1): 180–93. doi:10.1039/c0mb00088d. PMID   21042649.
  8. Trindade DM, Silva JC, Navarro MS, Torriani IC, Kobarg J (Aug 27, 2009). "Low-resolution structural studies of human Stanniocalcin-1". BMC Structural Biology. 9: 57. doi:10.1186/1472-6807-9-57. PMC   2744999 . PMID   19712479.

Further reading